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• W2276021482 abstract "Structure of the cAMP-dependent protein kinase catalytic subunit, where the asparagine residue 326 was replaced with acrylodan-cystein conjugate to implement this fluorescence reporter group into the enzyme, was modeled by molecular dynamics (MD) method and the positioning of the dye molecule in protein structure was characterized at temperatures 300K, 500K and 700K. It was found that the acrylodan moiety, which fluorescence is very sensitive to solvating properties of its microenvironment, was located on the surface of the native protein at 300K that enabled its partial solvation with water. At high temperatures the protein structure significantly changed, as the secondary and tertiary structure elements were unfolded and these changes were sensitively reflected in positioning of the dye molecule. At 700K complete unfolding of the protein occurred and the reporter group was entirely expelled into water. However, at 500K an intermediate of the protein unfolding process was formed, where the fluorescence reporter group was directed towards the protein interior and buried in the core of the formed molten globule state. This different positioning of the reporter group was in agreement with the two different shifts of emission spectrum of the covalently bound acrylodan, observed in the unfolding process of the protein." @default.
• W2276021482 created "2016-06-24" @default.
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• W2276021482 date "2016-04-01" @default.
• W2276021482 modified "2023-10-17" @default.
• W2276021482 title "Computational modeling of acrylodan-labeled cAMP dependent protein kinase catalytic subunit unfolding" @default.
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• W2276021482 doi "https://doi.org/10.1016/j.compbiolchem.2016.01.004" @default.
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